کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
6292406 1302553 2007 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Plasmodium vivax: Molecular cloning, expression and characterization of glutathione S-transferase
موضوعات مرتبط
علوم زیستی و بیوفناوری ایمنی شناسی و میکروب شناسی انگل شناسی
پیش نمایش صفحه اول مقاله
Plasmodium vivax: Molecular cloning, expression and characterization of glutathione S-transferase
چکیده انگلیسی
Malaria parasite glutathione S-transferases (GSTs) are postulated to be essential for parasite survival by protecting the parasite against oxidative stress and buffering the detoxification of heme-binding compounds; therefore, GSTs are considered potential targets for drug development. In this study, we identified a Plasmodium vivax gene encoding GST (PvGST) and characterized the biochemical properties of the recombinant enzyme. The PvGST contained 618 bp that encoded 205 amino acids and shared a significant degree of sequence identity with GSTs from other Plasmodium species. The recombinant homodimeric enzyme had an approximate molecular mass of 50 kDa and exhibited GSH-conjugating and GSH-peroxidase activities towards various model substrates. The optimal pH for recombinant PvGST (rPvGST) activity was pH 8.0, and the enzyme was moderately unstable at 37 °C. The Km values of rPvGST with respect to GSH and CDNB were 0.17 ± 0.09 and 2.1 ± 0.4 mM, respectively. The significant sequence homology and similar biochemical properties of PvGST and Plasmodium falciparum GST (PfGST) indicate that they may have similar molecular structures. This information may be useful for the design of specific inhibitors for plasmodial GSTs as potential antimalarial drugs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Parasitology - Volume 116, Issue 4, August 2007, Pages 414-418
نویسندگان
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